Table 5.
Data from denaturation curves followed by fluorescence spectroscopy.
| Protein | Urea unfoldinga | ||
|---|---|---|---|
| D150% (M) | D250% (M) | D350% (M) | |
| Wild typeb | 3.19 ± 0.31b | 6.93 ± 0.06b | - |
| W387F | 1.72 ± 0.43 | 6.10 ± 0.19 | - |
| W387F-Y49W | 1.57 ± 0.38 | 5.53 ± 0.07 | - |
| W387F-Y72W | 0.44 ± 0.15 | 6.80 ± 0.57 | - |
| W387F-Y85W | 0.83 ± 0.26 | 7.14 ± 0.13 | - |
| W387F-Y120W | 4.10 ± 0.39 | 6.19 ± 0.12 | - |
| W387F-Y170W | 0.78 ± 0.05 | 6.81 ± 0.04 | - |
| W387F-Y226W | 4.72 ± 0.26 | 6.66 ± 0.08 | - |
| W387F-Y233W | 1.12 ± 0.16 | 4.23 ± 0.05 | 7.44 ± 0.15 |
| W387F-Y255W | 3.13 ± 0.29 | 6.49 ± 0.09 | - |
| W387F-Y267W | 2.64 ± 0.40 | 6.07 ± 0.05 | - |
| W387F-Y273W | 1.03 ± 0..51 | 5.43 ± 0.17 | - |
| W387F-Y323W | 3.18 ± 0.22 | 5.56 ± 0.05 | - |
| W387F-Y344W | 2.69 ± 0.62 | 5.69 ± 0.09 | |
| W387F-Y371W | 6.81 ± 0.07 | - | - |
a
Mj-MAT wild type and mutants were incubated in the presence of urea and the fluorescent properties of each protein were then analyzed at 50 μg/ml upon excitation at 275 nm for W387F and 295 nm for the rest of the mutants. The table shows the mean ± SD of D50% from a typical experiment for each case.
b
Data from table 2